Biophysical Journal
Volume 118, Issue 2, 21 January 2020, Pages 352-365
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Article
Structure of an Unfolding Intermediate of an RRM Domain of ETR-3 Reveals Its Native-like Fold

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Abstract

Prevalence of one or more partially folded intermediates during protein unfolding with different secondary and ternary conformations has been identified as an integral character of protein unfolding. These transition-state species need to be characterized structurally for elucidation of their folding pathways. We have determined the three-dimensional structure of an intermediate state with increased conformational space sampling under urea-denaturing condition. The protein unfolds completely at 10 M urea but retains residual secondary structural propensities with restricted motion. Here, we describe the native state, observable intermediate state, and unfolded state for ETR-3 RRM-3, which has canonical RRM fold. These observations can shed more light on unfolding events for RRM-containing proteins.

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Harshesh Bhatt and Akshay Kumar Ganguly contributed equally to this work.Harshesh Bhatt’s present address is Lamarck Diagnostics, Kitchener, Ontario, Canada.

Akshay Kumar Ganguly’s present address is Sysmex Corporation, Nishi-ku, Kobe, Hyogo Prefecture, Japan.Editor: Doug Barrick.